Disruption of cell membranes by amyloid proteins is thought to be one of the major components of amyloid toxicity. However, the detailed mechanism by which the cell death occurs is not fully understood. Recent studies have demonstrated that membrane disruption by amyloid proteins occurs by a two-step process: initial ion-selective pore formation followed by nonspecific fragmentation of the membrane during amyloid aggregation. Our research in this area is focused on amyloid-beta related to Alzheimer’s disease and Islet amyloid polypeptide protein (IAPP, also known as amylin) implicated in type II diabetes. High-resolution structural and mechanistic insights on the formation of early oligomeric intermediates, pores and membrane fragmentation will be presented. Effect of amyloid-polyphenol interactions that could aid in the design of amyloid inhibitors will also be discussed. References: 1. Brender et al., Acc. Chem. Res. 2012, 45, 454-62. 2. Koler et al., Chem. Soc. Rev. 2014, 43, 6692-6700.

High resolution insights on the membrane mediated amyloid aggregation

249th National Meeting (2015)

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